Abstract
Inhibitory treatment by acetate, followed by illumination and rapid freezing, is known to trap the S2Y(z)· state of the O2-evolving complex (OEC) in photosystem II (PS II). An EPR spectrum of this state exhibits broad split signals due to the interaction of the tyrosyl radical, Y(z)·, with the S = 1/2 S2 state of the Mn4 cluster. We present a novel approach to analyze S2Y(z)· spectra of one-dimensionally (1-D) oriented acetate- inhibited PS II membranes to determine the magnitude and relative orientation of the S2Y(z)· dipolar vector within the membrane. Although there exists a vast body of EPR data on isolated spins in oriented membrane sheets, the present study is the first of its kind on dipolar-coupled electron spin pairs in such systems. We demonstrate the feasibility of the technique and establish a rigorous treatment to account for the disorder present in partially oriented 1-D membrane preparations. We find that (i) the point-dipole distance between Y(z)· and the Mn4 cluster is 7.9 ± 0.2 Å, (ii) the angle between the interspin vector and the thylakoid membrane normal is 75°, (iii) the g(z)-axis of the Mn4 cluster is 70°away from the membrane normal and 35°away from the interspin vector, and (iv) the exchange interaction between the two spins is -275 x 10-4 cm-1, which is antiferromagnetic. Due to the sensitivity of EPR line shapes of oriented spin-coupled pairs to the interspin distance, the present study imposes a tighter constraint on the Y(z)-Mn4 point-dipole distance than obtained from randomly oriented samples. The geometric constraints obtained from the 1-D oriented sample are combined with published models of the structure of Mn- depleted PS II to propose a location of the Mn4 cluster. A structure in which Y(z) is hydrogen bonded to a manganese-bound hydroxide ligand is consistent with available data and favors maximal orbital overlap between the two redox center that would facilitate direct electron- and proton-transfer steps.
| Original language | English |
|---|---|
| Pages (from-to) | 12758-12767 |
| Number of pages | 10 |
| Journal | Biochemistry |
| Volume | 38 |
| Issue number | 39 |
| DOIs | |
| Publication status | Published - Sep 28 1999 |
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ASJC Scopus subject areas
- Biochemistry
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Orientation of the tetranuclear manganese cluster and tyrosine Z in the O2-evolving complex of photosystem II : An EPR study of the S2Y(z)· state in oriented acetate-inhibited photosystem II membranes. / Lakshmi, K. V.; Eaton, Sandra S.; Eaton, Gareth R.; Brudvig, Gary W.
In: Biochemistry, Vol. 38, No. 39, 28.09.1999, p. 12758-12767.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Orientation of the tetranuclear manganese cluster and tyrosine Z in the O2-evolving complex of photosystem II
T2 - An EPR study of the S2Y(z)· state in oriented acetate-inhibited photosystem II membranes
AU - Lakshmi, K. V.
AU - Eaton, Sandra S.
AU - Eaton, Gareth R.
AU - Brudvig, Gary W
PY - 1999/9/28
Y1 - 1999/9/28
N2 - Inhibitory treatment by acetate, followed by illumination and rapid freezing, is known to trap the S2Y(z)· state of the O2-evolving complex (OEC) in photosystem II (PS II). An EPR spectrum of this state exhibits broad split signals due to the interaction of the tyrosyl radical, Y(z)·, with the S = 1/2 S2 state of the Mn4 cluster. We present a novel approach to analyze S2Y(z)· spectra of one-dimensionally (1-D) oriented acetate- inhibited PS II membranes to determine the magnitude and relative orientation of the S2Y(z)· dipolar vector within the membrane. Although there exists a vast body of EPR data on isolated spins in oriented membrane sheets, the present study is the first of its kind on dipolar-coupled electron spin pairs in such systems. We demonstrate the feasibility of the technique and establish a rigorous treatment to account for the disorder present in partially oriented 1-D membrane preparations. We find that (i) the point-dipole distance between Y(z)· and the Mn4 cluster is 7.9 ± 0.2 Å, (ii) the angle between the interspin vector and the thylakoid membrane normal is 75°, (iii) the g(z)-axis of the Mn4 cluster is 70°away from the membrane normal and 35°away from the interspin vector, and (iv) the exchange interaction between the two spins is -275 x 10-4 cm-1, which is antiferromagnetic. Due to the sensitivity of EPR line shapes of oriented spin-coupled pairs to the interspin distance, the present study imposes a tighter constraint on the Y(z)-Mn4 point-dipole distance than obtained from randomly oriented samples. The geometric constraints obtained from the 1-D oriented sample are combined with published models of the structure of Mn- depleted PS II to propose a location of the Mn4 cluster. A structure in which Y(z) is hydrogen bonded to a manganese-bound hydroxide ligand is consistent with available data and favors maximal orbital overlap between the two redox center that would facilitate direct electron- and proton-transfer steps.
AB - Inhibitory treatment by acetate, followed by illumination and rapid freezing, is known to trap the S2Y(z)· state of the O2-evolving complex (OEC) in photosystem II (PS II). An EPR spectrum of this state exhibits broad split signals due to the interaction of the tyrosyl radical, Y(z)·, with the S = 1/2 S2 state of the Mn4 cluster. We present a novel approach to analyze S2Y(z)· spectra of one-dimensionally (1-D) oriented acetate- inhibited PS II membranes to determine the magnitude and relative orientation of the S2Y(z)· dipolar vector within the membrane. Although there exists a vast body of EPR data on isolated spins in oriented membrane sheets, the present study is the first of its kind on dipolar-coupled electron spin pairs in such systems. We demonstrate the feasibility of the technique and establish a rigorous treatment to account for the disorder present in partially oriented 1-D membrane preparations. We find that (i) the point-dipole distance between Y(z)· and the Mn4 cluster is 7.9 ± 0.2 Å, (ii) the angle between the interspin vector and the thylakoid membrane normal is 75°, (iii) the g(z)-axis of the Mn4 cluster is 70°away from the membrane normal and 35°away from the interspin vector, and (iv) the exchange interaction between the two spins is -275 x 10-4 cm-1, which is antiferromagnetic. Due to the sensitivity of EPR line shapes of oriented spin-coupled pairs to the interspin distance, the present study imposes a tighter constraint on the Y(z)-Mn4 point-dipole distance than obtained from randomly oriented samples. The geometric constraints obtained from the 1-D oriented sample are combined with published models of the structure of Mn- depleted PS II to propose a location of the Mn4 cluster. A structure in which Y(z) is hydrogen bonded to a manganese-bound hydroxide ligand is consistent with available data and favors maximal orbital overlap between the two redox center that would facilitate direct electron- and proton-transfer steps.
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U2 - 10.1021/bi990780s
DO - 10.1021/bi990780s
M3 - Article
C2 - 10504246
AN - SCOPUS:0033613240
VL - 38
SP - 12758
EP - 12767
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 39
ER -